位置:成果数据库 > 期刊 > 期刊详情页
Orientation of the peptide formation of N-phosphoryl amino acids in solution
  • ISSN号:1004-132X
  • 期刊名称:《中国机械工程》
  • 时间:0
  • 分类:O623[理学—有机化学;理学—化学]
  • 作者机构:[1]Tsing Hua Univ, Sch Life Sci & Engn, Dept Chem, Bioorgan Phosphorus Chem Lab, Beijing 100084, Peoples R China, [2]Chinese Acad Sci, Inst Biophys, Ctr Biol Mol, Natl Lab Biomacromol, Beijing 100101, Peoples R China
  • 相关基金:the National Natural Science Foundation of China (Grant Nos. 20072023 and 20175026);the Teaching and Research Award Program for Outstanding Young Teachers in Higher Education Institute of Ministry of Education of China
中文摘要:

The peptide formation of N-phosphoryl aminoacids with amino acids proceeds in aqueous solution withoutany coupling reagents. After being separated in sephadex gelcolumn, the phosphoryl dipeptides were analyzed by theelectrospray ionization tandem mass spectrometry (ESIMS/MS). The result demonstrates that phosphoryl dipeptideswere datected in all the reaction systems. It is found tkat theformation of N-phosphoryl dipeptides is oriented: theN-terminal amino acid residues of the N-phosphoryl dipep-tides are from N-phosphoryl amino acids, and the peptideelongation happened at the C-terminal. Only adipeptide, noβ-dipeptide, is formed in the N-phosphoryl dipeptides,showing that α-carboxylic group is activated selectively byN-pbosphorylation. Theoretical calculation shows that thepeptide formation of N-phosphoryl amino acids might hap-pen through a pentu-coordinate carboxylic-phosphoric in-termediate in solution. These results might give some clues tothe stlidy on the origin of proteins and protein biosynthe

英文摘要:

The peptide formation of N-phosphoryl amino acids with amino acids proceeds in aqueous solution without any coupling reagents. After being separated in sephadex gel column, the phosphoryl dipeptides were analyzed by the electrospray ionization tandem mass spectrometry (ESIMS/ MS). The result demonstrates that phosphoryl dipeptides were detected in all the reaction systems. It is found that the formation of N-phosphoryl dipeptides is oriented: the N-terminal amino acid residues of the N-phosphoryl dipeptides are from N-phosphoryl amino acids, and the peptide elongation happened at the C-terminal. Only a-dipeptide, no β-dipeptide, is formed in the N-phosphoryl dipeptides, showing that a-carboxylic group is activated selectively by N-phosphorylation. Theoretical calculation shows that the peptide formation of N-phosphoryl amino acids might happen through a penta-coordinate carboxylic-phosphoric intermediate in solution. These results might give some clues to the study on the origin of proteins and protein biosynthesis.

同期刊论文项目
同项目期刊论文
期刊信息
  • 《中国机械工程》
  • 中国科技核心期刊
  • 主管单位:中国科学技术协会
  • 主办单位:中国机械工程学会
  • 主编:董仕节
  • 地址:湖北工业大学772信箱
  • 邮编:430068
  • 邮箱:paper@cmemo.org.cn
  • 电话:027-87646802
  • 国际标准刊号:ISSN:1004-132X
  • 国内统一刊号:ISSN:42-1294/TH
  • 邮发代号:38-10
  • 获奖情况:
  • 1997年获中国科协期刊一等奖,第二届全国优秀科技...,机械行业优秀期刊一等奖,1999年获首届国家期刊奖,2001年获首届湖北十大名刊,中国期刊方阵“双高”期刊,2003第二届国家期刊奖提名奖,百种中国杰出学术期刊
  • 国内外数据库收录:
  • 俄罗斯文摘杂志,美国化学文摘(网络版),荷兰文摘与引文数据库,美国剑桥科学文摘,英国科学文摘数据库,日本日本科学技术振兴机构数据库,中国中国科技核心期刊,中国北大核心期刊(2004版),中国北大核心期刊(2008版),中国北大核心期刊(2011版),中国北大核心期刊(2014版),中国北大核心期刊(2000版)
  • 被引量:50788